Interactive animation of the structure of ATP
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.
Simplified view of the cellular metabolism
The cycles of synthesis and degradation of ATP; 2 and 1 represent input and output of energy, respectively.
A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.
Structure of adenosine triphosphate (ATP), a central intermediate in energy metabolism
This image shows a 360-degree rotation of a single, gas-phase magnesium-ATP chelate with a charge of −2. The anion was optimized at the UB3LYP/6-311++G(d,p) theoretical level and the atomic connectivity modified by the human optimizer to reflect the probable electronic structure.
The redox reactions of nicotinamide adenine dinucleotide.
Structure of a triacylglycerol lipid
An example of the Rossmann fold, a structural domain of a decarboxylase enzyme from the bacterium Staphylococcus epidermidis with a bound flavin mononucleotide cofactor.
This is a diagram depicting a large set of human metabolic pathways.
Glucose can exist in both a straight-chain and ring form.
Structure of the coenzyme acetyl-CoA.The transferable acetyl group is bonded to the sulfur atom at the extreme left.
The structure of iron-containing hemoglobin. The protein subunits are in red and blue, and the iron-containing heme groups in green. From.
A simplified outline of the catabolism of proteins, carbohydrates and fats
Mechanism of ATP synthase. ATP is shown in red, ADP and phosphate in pink and the rotating stalk subunit in black.
Plant cells (bounded by purple walls) filled with chloroplasts (green), which are the site of photosynthesis
Simplified version of the steroid synthesis pathway with the intermediates isopentenyl pyrophosphate (IPP), dimethylallyl pyrophosphate (DMAPP), geranyl pyrophosphate (GPP) and squalene shown. Some intermediates are omitted for clarity.
Effect of insulin on glucose uptake and metabolism. Insulin binds to its receptor (1), which in turn starts many protein activation cascades (2). These include: translocation of Glut-4 transporter to the plasma membrane and influx of glucose (3), glycogen synthesis (4), glycolysis (5) and fatty acid synthesis (6).
Evolutionary tree showing the common ancestry of organisms from all three domains of life. Bacteria are colored blue, eukaryotes red, and archaea green. Relative positions of some of the phyla included are shown around the tree.
Metabolic network of the Arabidopsis thaliana citric acid cycle. Enzymes and metabolites are shown as red squares and the interactions between them as black lines.
Aristotle's metabolism as an open flow model
Santorio Santorio in his steelyard balance, from Ars de statica medicina, first published 1614

When consumed in metabolic processes, it converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP).

- Adenosine triphosphate

It is also a precursor to DNA and RNA, and is used as a coenzyme.

- Adenosine triphosphate

Many contain the nucleotide adenosine monophosphate (AMP) as part of their structures, such as ATP, coenzyme A, FAD, and NAD+.

- Cofactor (biochemistry)

These group-transfer intermediates are called coenzymes.

- Metabolism

One central coenzyme is adenosine triphosphate (ATP), the universal energy currency of cells.

- Metabolism

Therefore, these cofactors are continuously recycled as part of metabolism.

- Cofactor (biochemistry)
Interactive animation of the structure of ATP

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The redox reactions of nicotinamide adenine dinucleotide.

Nicotinamide adenine dinucleotide

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The redox reactions of nicotinamide adenine dinucleotide.
UV absorption spectra of NAD and NADH.
Some metabolic pathways that synthesize and consume NAD in vertebrates. The abbreviations are defined in the text.
Salvage pathways use three precursors for NAD+.
Rossmann fold in part of the lactate dehydrogenase of Cryptosporidium parvum, showing NAD in red, beta sheets in yellow, and alpha helices in purple.
In this diagram, the hydride acceptor C4 carbon is shown at the top. When the nicotinamide ring lies in the plane of the page with the carboxy-amide to the right, as shown, the hydride donor lies either "above" or "below" the plane of the page. If "above" hydride transfer is class A, if "below" hydride transfer is class B.
A simplified outline of redox metabolism, showing how NAD and NADH link the citric acid cycle and oxidative phosphorylation.
The structure of cyclic ADP-ribose.
Arthur Harden, co-discoverer of NAD

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism.

This contrasts with eukaryotic DNA ligases, which use ATP to form the DNA-AMP intermediate.